期刊
PROTEIN SCIENCE
卷 21, 期 5, 页码 601-605出版社
WILEY-BLACKWELL
DOI: 10.1002/pro.2056
关键词
a-synuclein; Parkinson's disease; N-terminal acetylation; amyloid
资金
- NIH [5F31AG038110-02]
- Ellison Medical Foundation
The aggregation of the protein a-synuclein (AS) is critical to the pathogenesis of Parkinson's disease. Although generally described as an unstructured monomer, recent evidence suggests that the native form of AS may be an a-helical tetramer which resists aggregation. Here, we show that N-terminal acetylation in combination with a mild purification protocol results in an oligomeric form of AS with partial a-helical structure. N-terminal acetylation of AS could have important implications for both the native and pathological structures and functions of AS. Through our demonstration of a recombinant expression system, our results represent an important step toward biochemical and biophysical characterization of this potentially important form of AS.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据